Human aldehyde dehydrogenase: kinetic identification of the isozyme for which biogenic aldehydes and acetaldehyde compete.

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TitleHuman aldehyde dehydrogenase: kinetic identification of the isozyme for which biogenic aldehydes and acetaldehyde compete.
Publication TypeJournal Article
Year of Publication1986
AuthorsMackerell, AD, Blatter, EE, Pietruszko, R
JournalAlcohol Clin Exp Res
Volume10
Issue3
Pagination266-70
Date Published1986 Jun
ISSN0145-6008
KeywordsAcetaldehyde, Aldehyde Dehydrogenase, Aldehydes, Catalysis, Cytoplasm, Humans, Isoenzymes, Kinetics, Liver, Mitochondria, Liver, Substrate Specificity
Abstract

Michaelis constants and maximal velocities for phenylacetaldehyde (a metabolite of phenylethylamine), 3,4-dihydroxyphenylacetaldehyde (a metabolite of dopamine), 5-hydroxyindole acetaldehyde (a metabolite of serotonin), and 3,4-dihydroxyphenylglycolaldehyde (a metabolite of epinephrine and norepinephrine) have been determined for both cytoplasmic (E1) and mitochondrial (E2) isozymes of human liver aldehyde dehydrogenase (EC 1.2.1.3). Kinetic constants with biogenic aldehydes have never been previously determined for individual homogeneous isozymes of aldehyde dehydrogenase from any species. Mathematical treatment of these constants suggests that competition with acetaldehyde during alcohol metabolism would severely inhibit dehydrogenation of biogenic aldehydes with the mitochondrial and not the cytoplasmic isozyme of human liver aldehyde dehydrogenase.

Alternate JournalAlcohol. Clin. Exp. Res.
PubMed ID3526948
Grant ListAA00186 / AA / NIAAA NIH HHS / United States
K02 AA00046 / AA / NIAAA NIH HHS / United States